Information on EC 1.1.2.7 -

Information on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c):

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EC NUMBER	COMMENTARY
1.1.2.7	-

RECOMMENDED NAME	GeneOntology No.
methanol dehydrogenase (cytochrome c)	GO:0052933

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		-	-	-	-
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		active site structure with bound cofactor, the reduced pyrroloquinoline quinone (PQQ) transfers two electrons in single electron-transfer steps to cytochrome cL, creating a semiquinone form of the prosthetic group after the first electron transfer, electron transfer via enzyme residues Cys104, Asp105, and Asn52	Methylobacterium extorquens	-	671068
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		addition–elimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387	Methylophilus methylotrophus	-	673047
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved	Hyphomicrobium denitrificans	-	673048
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		detailed mechanism of methanol oxidation involving residues Asp297 and Glu171, structure-activity analysis by quantum mechanics and molecular mechanics, QM/MM, selfconsistent-charge density-functional tight-binding, SCC-DFTB, and molecular dynamics, the transition state involves Glu171-CO2- as general base	Methylophilus methylotrophus	-	676902
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		detailed reaction mechanism with direct hydride transfe, Glu177 plays the role of general base catalyst	Methylobacterium extorquens	-	684666
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		detailed reaction mechanism with direct hydride transfer	Methylophilus sp.	-	684666
a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL		catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview	Methylobacterium extorquens	-	687993

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

PATHWAY	KEGG Link	MetaCyc Link
methanol oxidation to formaldehyde I	-	PWY-6966

SYSTEMATIC NAME

IUBMB Comments

methanol:cytochrome c oxidoreductase

A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulphate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulphide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Hd-MDH	Hyphomicrobium denitrificans	-	-	667721
MDH	Hyphomicrobium denitrificans	-	-	667721, 673048
MDH	Methylobacterium extorquens	-	-	670785, 671068, 687993, 688333, 690794
MDH	Methylophilus methylotrophus	-	-	673047, 676902, 687993
MDH	Methylosinus sp.	-	-	687432
MDH2	Methylibium petroleiphilum	-	Mdh2 is a type I alcohol dehydrogenase	687417
MEDH	Methylophilus sp.	-	-	685050
MEDH	Methylophilus methylotrophus	-	-	687486
methanol dehydrogenase	Hyphomicrobium denitrificans	-	-	667721, 673048
methanol dehydrogenase	Methylobacterium extorquens	-	-	670785, 671068, 684666, 684947, 684948, 685313, 687993, 688333, 689139, 690794
methanol dehydrogenase	Methylophilus methylotrophus	-	-	673047, 687486, 687993
methanol dehydrogenase	Methylophilus sp.	-	-	684666, 685050, 685313
pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase	Methylibium petroleiphilum, Methyloversatilis universalis	-	-	687417
QH-ADH	Methylobacterium extorquens, Methylophilus methylotrophus	-	-	687993
quinohemoprotein (type II) alcohol dehydrogenase	Methylobacterium extorquens, Methylophilus sp.	-	-	685313
quinohemoprotein alcohol dehydrogenases	Methylobacterium extorquens, Methylophilus methylotrophus	-	-	687993
quinoprotein alcohol dehydrogenase	Methylobacterium extorquens, Methylophilus methylotrophus	-	-	687993
quinoprotein dehydrogenase	Methylobacterium extorquens, Methylophilus sp.	-	-	684666
quinoprotein methanol dehydrogenase	Methylophilus methylotrophus	-	-	676902, 689815, 689818
quinoprotein methanol dehydrogenase	Methylobacterium extorquens	-	-	684947, 684950, 689139, 690095
methanol dehydrogenase	Methylosinus sp.	-	-	687432
additional information	Methyloversatilis universalis	-	Mdh2 is a type I alcohol dehydrogenase	687417

CAS REGISTRY NUMBER	COMMENTARY
No entries in this field

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Hyphomicrobium denitrificans	strain A3151	667721, 673048	-	-
Methylibium petroleiphilum	strain PM1, gene mdh2, the organism lacks gene mxaFI, which encodes the wide-spread dimeric methanol dehydrogenase	687417	-	-
Methylobacterium extorquens	-	671068, 712855	-	-
Methylobacterium extorquens	P16027 (large subunit, alpha) and P14775 (small subunit, beta)	684666, 685313, 687993, 688333, 689139, 690095, 690794	P16027 and P14775	UniProt
Methylobacterium extorquens	P16027 (large subunit, alpha) and P14775 (small subunit, beta); gene mxaA	684950	P16027 and P14775	UniProt
Methylobacterium extorquens	P16027 (large subunit, alpha) and P14775 (small subunit, beta); strain AM1	684948	P16027 and P14775	UniProt
Methylobacterium extorquens	P16027 (large subunit, alpha) and P14775 (small subunit, beta); strain AM1, ATCC 14718	670785	P16027 and P14775	UniProt
Methylobacterium extorquens	P16027 (large subunit, alpha) and P14775 (small subunit, beta); strain NCIMB 9133	684947	P16027 and P14775	UniProt
Methylobacterium extorquens NCIMB 9133	P16027 (large subunit, alpha) and P14775 (small subunit, beta); strain NCIMB 9133	684947	P16027 and P14775	UniProt
Methylophilus methylotrophus	P38539 (large subunit, alpha) and P38540 (small subunit, beta)	676902, 687993	P38539 and P38540	UniProt
Methylophilus methylotrophus	P38539 (large subunit, alpha) and P38540 (small subunit, beta); strain W3A1	687486, 689815, 689818	P38539 and P38540	UniProt
Methylophilus methylotrophus	strain W3A1	673047	-	-
Methylophilus sp.	-	684666, 685313	-	-
Methylophilus sp.	strain W3A1	685050	-	-
Methylosinus sp.	strain WI 14	687432	-	-
Methyloversatilis universalis	strain FAM5, gene mdh2, the organism lacks gene mxaFI, which encodes the wide-spread dimeric methanol dehydrogenase	687417	-	-
Pseudomonas sp. AM1	P16027 (large subunit, alpha) and P14775 (small subunit, beta); strain AM1	684948	P16027 and P14775	UniProt
Rubrivivax gelatinosus PM1	strain PM1, gene mdh2, the organism lacks gene mxaFI, which encodes the wide-spread dimeric methanol dehydrogenase	687417	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
butanol + 2,6-dichlorophenolindophenol	butyraldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
ethanol + 2,6-dichlorophenolindophenol	acetaldehyde + reduced 2,6-dichlorophenolindophenol		Methyloversatilis universalis, Methylibium petroleiphilum	-	reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate	687417	-	-	?
ethanol + 2,6-dichlorophenolindophenol	acetaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
heptanol + 2,6-dichlorophenolindophenol	heptaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
hexanol + 2,6-dichlorophenolindophenol	hexaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
methanol + 2,6-dichlorophenolindophenol	formaldehyde + reduced 2,6-dichlorophenolindophenol		Methyloversatilis universalis, Methylibium petroleiphilum	-	reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate	687417	-	-	?
methanol + 2,6-dichlorophenolindophenol	formaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
methanol + cytochrome cL	formaldehyde + reduced cytochrome cL		Hyphomicrobium denitrificans	-	way of electron transfer from methanol to O2, overview	667721	-	-	?
methanol + ferricytochrome cL	acetaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	-	689139	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylophilus sp.	-	-	684666, 685313	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Hyphomicrobium denitrificans	-	-	667721	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylosinus sp.	-	-	687432	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	P16027 and P14775	-	684666, 684950	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	-	685313, 688333, 690095	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	terminal electron acceptor is cytochrome cL	671068	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylophilus sp.	-	MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol	684666	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	P16027 and P14775	MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol	684666	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL	688333	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	P16027 and P14775	the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview	684948	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylophilus sp., Methylobacterium extorquens	-	periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen	685313	-	-	?
n-butanol + 2,6-dichlorophenolindophenol	butyraldehyde + reduced 2,6-dichlorophenolindophenol		Methyloversatilis universalis, Methylibium petroleiphilum	-	reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate	687417	-	-	?
n-propanol + 2,6-dichlorophenolindophenol	propionaldehyde + reduced 2,6-dichlorophenolindophenol		Methyloversatilis universalis, Methylibium petroleiphilum	-	reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate	687417	-	-	?
octanol + 2,6-dichlorophenolindophenol	octaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
pentanol + 2,6-dichlorophenolindophenol	pentaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
propanol + 2,6-dichlorophenolindophenol	propionaldehyde + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
sorbic alcohol + 2,6-dichlorophenolindophenol	? + reduced 2,6-dichlorophenolindophenol		Methylosinus sp.	-	with phenazine methosulfate	687432	-	-	?
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH	671068	-	-	?
additional information	?	-	Methyloversatilis universalis, Methylibium petroleiphilum	-	methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria	687417	-	-	-
additional information	?	-	Methylobacterium extorquens	-	active site structure with important disulfide bridge of Cys103-Cys104, overview	690095	-	-	-
additional information	?	-	Methylobacterium extorquens	-	active site structure, the Cys103-Cys104 disulfide bridge plays a role in the electron transfer during catalysis, overview	689139	-	-	-
additional information	?	-	Methylosinus sp.	-	broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes	687432	-	-	-
additional information	?	-	Methylobacterium extorquens	-	MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview	690794	-	-	-
additional information	?	-	Methylobacterium extorquens	-	oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor	687993	-	-	-
additional information	?	-	Methylophilus methylotrophus	-	oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor, catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview	687993	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
methanol + cytochrome cL	formaldehyde + reduced cytochrome cL		Hyphomicrobium denitrificans	-	way of electron transfer from methanol to O2, overview	667721	-	-
methanol + ferricytochrome cL	acetaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	-	689139	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Hyphomicrobium denitrificans	-	-	667721	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylosinus sp.	-	-	687432	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	P16027 and P14775	-	684950	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	-	688333, 690095	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylophilus sp.	-	MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol	684666	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	P16027 and P14775	MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol	684666	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylophilus sp., Methylobacterium extorquens	-	periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen	685313	-	-
methanol + ferricytochrome cL	formaldehyde + ferrocytochrome cL		Methylobacterium extorquens	-	the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH	671068	-	-
additional information	?	-	Methyloversatilis universalis, Methylibium petroleiphilum	-	methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria	687417	-	-
additional information	?	-	Methylobacterium extorquens	-	MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview	690794	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2,7,9-tricarboxypyrroloquinoline quinone	Methylophilus methylotrophus	-	PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview	689818	2D-image
cytochrome cL	Hyphomicrobium denitrificans	-	-	667721	-
cytochrome cL	Methylobacterium extorquens	-	-	684666, 684948, 690794	-
cytochrome cL	Methylophilus sp.	-	-	684666	-
cytochrome cL	Methylobacterium extorquens	P16027 and P14775	electron acceptor	684950	-
cytochrome cL	Methylobacterium extorquens	-	flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding and crystal structure determination and analysis at 1.6 A resolution, contains a disulfide bridge that tethers the long C-terminal extension to the body of the structure, overview	688333	-
phenazine methosulfate	Methylibium petroleiphilum	-	mediates reduction of 2,6-dichlorophenolindophenol	687417	2D-image
phenazine methosulfate	Methyloversatilis universalis	-	mediates reduction of 2,6-dichlorophenol-indophenol	687417	2D-image
pyrroloquinoline quinone	Hyphomicrobium denitrificans	-	enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer	667721	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	P16027 and P14775	i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity	670785	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview	671068	2D-image
pyrroloquinoline quinone	Methylophilus methylotrophus	-	i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104	673047	2D-image
pyrroloquinoline quinone	Hyphomicrobium denitrificans	-	bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview	673048	2D-image
pyrroloquinoline quinone	Methylophilus methylotrophus	-	-	676902	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview	684666	2D-image
pyrroloquinoline quinone	Methylophilus sp.	-	PQQ, is the only prosthetic group	684666	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	P16027 and P14775	PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview	684947	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	P16027 and P14775	PQQ	684948	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	P16027 and P14775	PQQ, prosthetic group	684950	2D-image
pyrroloquinoline quinone	Methylophilus sp.	-	PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview	685050	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261	685313	2D-image
pyrroloquinoline quinone	Methylophilus sp.	-	PQQ, binding structure at the active site	685313	2D-image
pyrroloquinoline quinone	Methylibium petroleiphilum, Methyloversatilis universalis	-	dependent on	687417	2D-image
pyrroloquinoline quinone	Methylosinus sp.	-	prosthetic group, 1.3 molecules per enzyme molecule	687432	2D-image
pyrroloquinoline quinone	Methylophilus methylotrophus	-	the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule	687486	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens, Methylophilus methylotrophus	-	i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview	687993	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure	688333	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	binding structure in the active site, overview	689139	2D-image
pyrroloquinoline quinone	Methylophilus methylotrophus	-	PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview	689815	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group	690095	2D-image
pyrroloquinoline quinone	Methylobacterium extorquens	-	PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure	690794	2D-image
Heme c	Methylobacterium extorquens	-	part of cytochrome cL	688333	2D-image
additional information	Methylobacterium extorquens	-	an NAD(P)-independent enzyme	684948, 690794	-

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ba2+	Methylobacterium extorquens	-	can substitute for Ca2+, Ba-MDH has twice the maximum activity of the Ca-MDH but with a much lower affinity for its substrates	684666
Ba2+	Methylobacterium extorquens	P16027 and P14775	Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Ba2+ shows 102% of the activity with Ca2+	684950
Ba2+	Methylobacterium extorquens	-	modeling of Ba2+-containing MDH active site to investigate the proposed addition-elimination and hydride-transfer methanol oxidation mechanisms. For both mechanisms, almost all the free-energy barriers associated with all of the steps are reduced in the presence of Ba2+-MDH, and they are kinetically feasible. The free energy barriers for methanol oxidation by Ba2+-MDH, particularly for the rate-limiting steps of both mechanisms, are almost half the corresponding barriers calculated for the case of Ca2+-MDH	712855
Ca2+	Methylobacterium extorquens	P16027 and P14775	bound to the active site, required for catalytic activity	670785
Ca2+	Methylobacterium extorquens	-	required, bound at the active site, interaction with the cofactor and the active site residues Arg331, Asp303, and Glu177, but not Asn261, structure overview	671068
Ca2+	Methylophilus methylotrophus	-	required for catalytic activity, binding structure, overview	673047
Ca2+	Hyphomicrobium denitrificans	-	absolutely required, 1.43 Ca2+ per enzyme tetramer, tightly bound to the active site, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview, Ca2+-free enzyme is inactive	673048
Ca2+	Methylophilus methylotrophus	-	required	676902
Ca2+	Methylobacterium extorquens, Methylophilus sp.	-	the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms	684666
Ca2+	Methylobacterium extorquens	P16027 and P14775	one molecule of Ca2+ per enzyme tetramer. Ca2+ is directly or indirectly involved in the biding of pyrroloquinoline quinone. Methanol oxidation mutants MoxA-, K- and L- contain no Ca2+. The MoxA, K and L proteins may be involved in maintaining a high Ca2+ concentration in the periplasm. It is more likely, that they fill a chaperone function, stabilizing a configuration of methanol dehydrogenase which permits incorporation of low concentrations of Ca2+ into the protein	684947
Ca2+	Methylobacterium extorquens	P16027 and P14775	one molecule per enzyme alpha-subunit. Neither the quinone form of pyrroloquinoline quinone, nor the disulfide ring or its reduced form are absolutely essential for calcium incorporation into the active site	684948
Ca2+	Methylobacterium extorquens	P16027 and P14775	2 Ca2+ ions are irreversibly incorporated per alpha2beta2 tetramer. Calcium can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+	684950
Ca2+	Methylophilus sp.	-	Ca2+ is six-coordinated with bonds to 05, N6, and carboxyl oxygen 07A of PQQ, the two carboxyl oxygen atoms of Glu171, and the side-chain oxygen of Asn255, binding structure, overview	685050
Ca2+	Methylobacterium extorquens	-	binding structure at the active site, overview, the active site contains a single Ca2+ ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261	685313
Ca2+	Methylophilus sp.	-	binding structure at the active site, overview	685313
Ca2+	Methylobacterium extorquens, Methylophilus methylotrophus	-	required for activity, functional role analysis, overview	687993
Ca2+	Methylobacterium extorquens	-	tightly bound close to the inner heme propionate, Ca2+ is involved in stabilization of the redox potential, and is important in the flow of electrons from reduced pyrroloquinoline quinone in methanol dehydrogenase to the heme of cytochrome cL	688333
Ca2+	Methylobacterium extorquens	-	binding strucure in the active site, overview	689139
Ca2+	Methylophilus methylotrophus	-	required for activity, overview	689815
Ca2+	Methylophilus methylotrophus	-	required for activity	689818
Ca2+	Methylobacterium extorquens	-	required for activity, one of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group	690095
Ca2+	Methylobacterium extorquens	-	one molecule per enzyme alpha-subunit, binding involves Glu177 and Asn261, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism	690794
Sr2+	Methylobacterium extorquens	P16027 and P14775	Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Sr2+ shows 94% of the activity with Ca2+	684950
Fe2+	Methylobacterium extorquens	-	a cytochrome protein	684948, 690794
additional information	Methylobacterium extorquens	-	Mg2+ cannot substitute for Ca2+	671068

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Cu2+	Methylosinus sp.	-	38% inhibition at 0.1 mM	687432	2D-image
Cyclopropanol	Methylobacterium extorquens	P16027 and P14775	-	684947	2D-image
phenazine methosulfate	Methylosinus sp.	-	39% inhibition at 3 mM	687432	2D-image
Fe2+	Methylosinus sp.	-	complete inhibition at 1 mM	687432	2D-image
additional information	Methylosinus sp.	-	no or poor inhibition by Ca2+, Co2+, Li+, Mg2+, Mn2+, and KCN, EDTA, and DTE	687432	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ammonia	Methylobacterium extorquens, Methylophilus sp.	-	ammonia affects the rate-limiting step of breaking of the methyl C-H bond	685313	2D-image
Methylamine	Methylosinus sp.	-	can replace NH4+	687432	2D-image
NH4+	Methylosinus sp.	-	absolute requirement, NH4+ can be replaced by methylamine but not by di- or triamines	687432	2D-image
NH4Cl	Methylibium petroleiphilum, Methyloversatilis universalis	-	essential activator	687417	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
6.38	-	butanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
0.01	-	ethanol	Methylibium petroleiphilum	-	pH 7.5, 22°C	687417	2D-image
0.05	-	ethanol	Methyloversatilis universalis	-	pH 7.5, 22°C	687417	2D-image
3.58	-	ethanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
0.0003	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 5.5, ionic strength: 0.0160 M, steady-state kinetic parameter	667721	2D-image
0.0006	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 6.0, ionic strength: 0.0172 M, steady-state kinetic parameter	667721	2D-image
0.0011	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 6.5, ionic strength: 0.0183 M, steady-state kinetic parameter	667721	2D-image
0.0026	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 5.0, ionic strength: 0.0181 M, steady-state kinetic parameter	667721	2D-image
0.009	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 4.5, ionic strength: 0.0168 M, steady-state kinetic parameter	667721	2D-image
0.105	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 7.0, ionic strength: 0.0198 M, steady-state kinetic parameter	667721	2D-image
0.58	-	Heptanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
0.79	-	Hexanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
0.01	-	methanol	Methyloversatilis universalis	-	pH 7.5, 22°C	687417	2D-image
0.29	-	methanol	Methylibium petroleiphilum	-	pH 7.5, 22°C	687417	2D-image
0.01	-	n-butanol	Methylibium petroleiphilum	-	pH 7.5, 22°C	687417	2D-image
0.5	-	n-butanol	Methyloversatilis universalis	-	pH 7.5, 22°C	687417	2D-image
0.09	-	n-Propanol	Methylibium petroleiphilum	-	pH 7.5, 22°C	687417	2D-image
0.5	-	n-Propanol	Methyloversatilis universalis	-	pH 7.5, 22°C	687417	2D-image
0.65	-	Octanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
1.34	-	Pentanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor 2,6-dichlorophenolindophenol	687432	2D-image
3.69	-	Propanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
0.18	-	sorbic alcohol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
0.45	-	methanol	Methylosinus sp.	-	pH 9.0, 57°C, acceptor: 2,6-dichlorophenolindophenol	687432	2D-image
additional information	-	additional information	Hyphomicrobium denitrificans	-	steady-state and stopped-flow kinetics	667721	-
additional information	-	additional information	Methylophilus methylotrophus	-	thermodynamics	673047	-
additional information	-	additional information	Methylobacterium extorquens, Methylophilus sp.	-	steady-state analysis using stopped-flow kinetics, molecular dynamics, overview	684666	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.15	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 5.5, ionic strength: 0.0160 M, steady-state kinetic parameter	667721	2D-image
0.21	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 6.0, ionic strength: 0.0172 M, steady-state kinetic parameter	667721	2D-image
0.33	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 6.5, ionic strength: 0.0183 M, steady-state kinetic parameter	667721	2D-image
0.41	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 5.0, ionic strength: 0.0181 M, steady-state kinetic parameter	667721	2D-image
0.45	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 4.5, ionic strength: 0.0168 M, steady-state kinetic parameter	667721	2D-image
0.87	-	ferricytochrome cL	Hyphomicrobium denitrificans	-	pH 7.0, ionic strength: 0.0198 M, steady-state kinetic parameter	667721	2D-image
0.87	-	methanol	Hyphomicrobium denitrificans	-	pH 7.0, 25°C	667721	2D-image
additional information	-	additional information	Hyphomicrobium denitrificans	-	kcat at different pH, overview	667721	-

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.12	0.7	Hyphomicrobium denitrificans	-	dependent on pH, overview	667721
5.4	-	Methylobacterium extorquens	P16027 and P14775	purified enzyme	670785
6.12	-	Methylosinus sp.	-	purified enzyme	687432
13	-	Hyphomicrobium denitrificans	-	purified reconstituted Ca2+-enzyme	673048
18	-	Hyphomicrobium denitrificans	-	purified native Ca2+-enzyme	673048
additional information	-	Hyphomicrobium denitrificans	-	-	667721
additional information	-	Hyphomicrobium denitrificans	-	Ca2+-free enzyme is inactive	673048

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7	-	Hyphomicrobium denitrificans	-	-	667721
7	-	Methylobacterium extorquens	-	assay at	684666
7.5	-	Methylibium petroleiphilum, Methyloversatilis universalis	-	assay at	687417
9	-	Methylobacterium extorquens	P16027 and P14775	assay at	670785, 684947, 684948
9	-	Methylosinus sp.	-	-	687432
10	-	Methylobacterium extorquens	P16027 and P14775	about	684950

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7	10.5	Methylobacterium extorquens	P16027 and P14775	pH profile, overview	684950
7	9	Hyphomicrobium denitrificans	-	the enzyme oxidation step becomes rate-limiting at pH 9.0	667721

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
20	-	Methylobacterium extorquens	P16027 and P14775	assay at	684947, 684948
22	-	Methylibium petroleiphilum, Methyloversatilis universalis	-	assay at room temperature	687417
25	-	Hyphomicrobium denitrificans	-	assay at	667721
25	-	Methylobacterium extorquens	P16027 and P14775	assay at	684950
57	-	Methylosinus sp.	-	-	687432

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
8.8	-	Methylobacterium extorquens	P16027 and P14775	sequence calculation	670785

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
No entries in this field

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
periplasm	Methylobacterium extorquens	-	-	-	671068, 684666, 684950, 685313, 690095, 690794
periplasm	Methylophilus methylotrophus	-	-	-	673047, 687486
periplasm	Methylophilus sp.	-	-	-	684666, 685313
periplasm	Methylibium petroleiphilum, Methyloversatilis universalis	-	-	-	687417
soluble	Methylobacterium extorquens	-	-	-	684950, 690794
soluble	Methylosinus sp.	-	-	-	687432

PDB	SCOP	CATH	ORGANISM
No entries in this field

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
138000	-	Methylophilus methylotrophus	-	gel filtration	687486
140000	-	Methylosinus sp.	-	gel filtration	687432
148000	-	Hyphomicrobium denitrificans	-	-	667721

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Methylobacterium extorquens	P16027 and P14775	x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE	670785
dimer	Methylosinus sp.	-	2 * 70000, SDS-PAGE	687432
tetramer	Hyphomicrobium denitrificans	-	2 * 65000 + 2 * 9000; alpha2beta2 structure, subunit organization and structure, docking model, overview	667721
tetramer	Methylobacterium extorquens	-	alpha2beta2 subunit conposition, structure model of an alphabeta unit from crystal structure determination, overview	671068
tetramer	Methylophilus methylotrophus	-	2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination	673047
tetramer	Hyphomicrobium denitrificans	-	2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE	673048
tetramer	Methylobacterium extorquens	-	2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination	684666
tetramer	Methylobacterium extorquens	P16027 and P14775	alpha2beta2, comparison of wild-type and mutant enzyme structures, overview	684947
tetramer	Methylophilus sp.	-	heterotetramer, structure analysis and modelling, overview	685050
tetramer	Methylophilus methylotrophus	-	alpha2beta2	687486
tetramer	Methylobacterium extorquens	-	alpha2beta2, three-dimensional structure, modelling, overview	689139
tetramer	Methylobacterium extorquens	-	alpha2beta2, the alpha-subunit has an 8fold radial symmetry, with its eight 3-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond, subunit structures and interactions, overview	690095
tetramer	Methylobacterium extorquens	-	4 * 66000, alpha2beta2, crystal structure	690794
monomer	Methyloversatilis universalis	-	in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein	687417
additional information	Methylobacterium extorquens	-	the periplasmic protein contains both a PQQ-containing domain, folded into a beta-propeller fold, and a smaller cytochrome c domain, which is analogous to a typical class I c-type cytochrome, these two domains are connected via a proline-rich linker region, which lacks any secondary structure, structure model of the electron-transfer complex formed by MDH and cytochrome cL, overview	671068
additional information	Methylobacterium extorquens	-	the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond	684666
additional information	Methylibium petroleiphilum	-	in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methylibium petroleiphilum strain PM1 is a monosubunit protein	687417

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
enzyme or cytochrome cL, hanging drop vapour diffusion method, 16°C, 0.001 ml of 20 mg/mL enzyme or cofactor in 40 mM Tris-HCl buffer, pH 7.5, is mixed with an equal volume of precipitant colution containing 0.2 M potassium thiocyanate and 20% PEG 3350 for the enzyme crystallization, and 2 mM ZnSO4, 20% PEG 10000, and 100 mM HEPES, pH 7.3, for the crystallization of Cyt cL, 1 week to 1 month, X-ray diffraction structure determination and analysis at 1.98-2.5 A resolution; hanging-drop vapor diffusion method, X-ray structures of methanol dehydrogenase (Hd-MDH) and cytochrome cL at 2.5 A and 2.0 A resolution, respectively. Docking simulation between the coupled cytochrome cL molecules and the heterotetrameric methanol dehydrogenase	Hyphomicrobium denitrificans	-	667721
Ba2+-containing MDH active site model to investigate the two proposed addition-elimination and hydride-transfer methanol oxidation mechanisms	Methylobacterium extorquens	-	712855
crystal structure analysis	Methylobacterium extorquens	-	685313, 690794
purified holoenzyme, hanging-drop vapour-diffusion method, 3 ml of 15 mg/ml protein solution, 20 mM Tris buffer, pH 8.0, are placed on siliconized cover slips and mixed with an equal volume of well solution, the cover slip is sealed with high-vacuum grease over a 1 ml well containing 20% PEG 8000, pH 9.0, large crystals after two weeks, X-ray diffraction structure determination and analysis at 1.2 A resolution, modeling	Methylobacterium extorquens	-	671068
X-ray diffraction structure determination	Methylobacterium extorquens	-	684666
X-ray diffraction structure determination and analysis at 1.94 A resolution	Methylobacterium extorquens	-	690095
X-ray diffraction strcuture determination and analysis at 2.6 A resolution, multiple isomorphous replacement, modelling	Methylophilus methylotrophus	-	687486
crystal structure analysis	Methylophilus sp.	-	685313
crystal structure determination	Methylophilus sp.	-	684666

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
60	-	Methylosinus sp.	-	30 min, purified enzyme, loss of 25% activity	687432

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
EDTA, DTT, and Ca2+ are slightly stabilizing	Methylobacterium extorquens	P16027 and P14775	670785

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-80°C, purified native enzyme, 20 mM phosphate, pH 7.0, negligible loss of activity in 6 months	Methylobacterium extorquens	P16027 and P14775	670785
4°C, purified native enzyme, 20 mM phosphate, pH 7.0, loss of 80% activity within 1 week	Methylobacterium extorquens	P16027 and P14775	670785
-18°C, purified native enzyme, 0.05 M sodium phosphate buffer, pH 7.5, loss of 10% of activity after 1 month	Methylosinus sp.	-	687432
4°C, purified native enzyme, 0.05 M sodium phosphate buffer, pH 7.5, loss of 30% of activity after 24 h	Methylosinus sp.	-	687432

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Hyphomicrobium denitrificans	-	667721
Ca2+-containing and Ca2+-free enzymes from cell-free extracts by ion exchange and hydrophobic interaction chromatography	Hyphomicrobium denitrificans	-	673048
native enzyme 22fold from strain AM1 in a single cation exchange chromatographical step, followed by ultrafiltration and buffer exchange, over 97% purity	Methylobacterium extorquens	P16027 and P14775	670785
native enzyme 9fold to homogeneity by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography, followed by ultrafiltration and gel filtration	Methylosinus sp.	-	687432

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
DNA and amino acid sequence determination and analysis	Hyphomicrobium denitrificans	-	673048
gene mdh2, DNA and amino acid sequence determination and analysis, phylogenetic analysis	Methylibium petroleiphilum, Methyloversatilis universalis	-	687417

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	Hyphomicrobium denitrificans	-	preparation of an inactive Ca2+-free MDH-containing Hyphomicrobium denitrificans strain, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, elucidation of the Ca2+ ion elimination mechanism, overview	673048
additional information	Methylobacterium extorquens	P16027 and P14775	construction of Ca2+-lacking mutant enzymes MoxA-, MoxK-, and MoxL-, which possess a fully oxidized pyrroloquinoline quinone cofactor that is not in the semiquinone form, incubation in a calcium salt solution leads to full restoration of the mutant enzymes, the mutant enzymes show a cofactor binding defect and are insensitive to inhibitor cyclopropanol, comparison of wild-type and mutant enzyme structures, overview	684947
additional information	Methylobacterium extorquens	P16027 and P14775	a Ca2+-free enzyme mxaA mutant is inactive	684948
additional information	Methylobacterium extorquens	P16027 and P14775	construction of Ca2+-lacking, catalytically inactive mutant apoenzymes, reconstitution of the active holoenzyme by incorporation of two exogenous Ca2+ into the active sites of the alpha-subunits of the alpha2beta2 tetramer	684950
additional information	Methylobacterium extorquens	-	mutation of Cys103-Cys104, forming a disulfide brigde, leads to loss of catalytic activity	685313

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
incubation in a calcium salt solution leads to full restoration of the Ca2+-lacking mutant enzymes to active holoenzymes, overview	Methylobacterium extorquens	P16027 and P14775	684947
reconstitution of the active holoenzyme by incorporation of two exogenous Ca2+ into the active sites of the alpha-subunits of the alpha2beta2 tetramer, time course of Ca2+ incorporation, overview	Methylobacterium extorquens	P16027 and P14775	684950

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
667721	Nojiri, M.; Hira, D.; Yamaguchi, K.; Okajima, T.; Tanizawa, K.; Suzuki, S.	Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins	Biochemistry	45	3481-3492	2006	Hyphomicrobium denitrificans	PubMed
670785	Liu, Q.; Kirchhoff, J.R.; Faehnle, C.R.; Viola, R.E.; Hudson, R.A.	A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens	Protein Expr. Purif.	46	316-320	2006	Methylobacterium extorquens	PubMed
671068	Williams, P.A.; Coates, L.; Mohammed, F.; Gill, R.; Erskine, P.T.; Coker, A.; Wood, S.P.; Anthony, C.; Cooper, J.B.	The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens	Acta Crystallogr. Sect. D	D61	75-79	2005	Methylobacterium extorquens	PubMed
673047	Leopoldini, M.; Russo, N.; Toscano, M.	The preferred reaction path for the oxidation of methanol by PQQ-containing methanol dehydrogenase: addition-elimination versus hydride-transfer mechanism	Chem. Eur. J.	13	2109-2117	2007	Methylophilus methylotrophus	PubMed
673048	Nojiri, M.; Hira, D.; Yamaguchi, K.; Okajima, T.; Tanizawa, K.; Suzuki, S.	Preparation and characterization of Ca2+-free methanol dehydrogenase from Hyphomicrobium denitrificans A3151	Chem. Lett.	34	1036-1037	2005	Hyphomicrobium denitrificans	-
676902	Zhang, X.; Reddy, S.Y.; Bruice, T.C.	Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase	Proc. Natl. Acad. Sci. USA	104	745-749	2007	Methylophilus methylotrophus	PubMed
684666	Anthony, C.	The quinoprotein dehydrogenases for methanol and glucose	Arch. Biochem. Biophys.	428	2-9	2004	Methylobacterium extorquens, Methylophilus sp.	PubMed
684947	Richardson, I.W.; Anthony, C.	Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion	Biochem. J.	287	709-715	1992	Methylobacterium extorquens	PubMed
684948	Avezoux, A.; Goodwin, M.G.; Anthony, C.	The role of the novel disulphide ring in the active site of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens	Biochem. J.	307	735-741	1995	Methylobacterium extorquens	PubMed
684950	Goodwin, M.G.; Avezoux, A.; Dales, S.L.; Anthony, C.	Reconstitution of the quinoprotein methanol dehydrogenase from inactive Ca(2+)-free enzyme with Ca2+, Sr2+ or Ba2+	Biochem. J.	319	839-842	1996	Methylobacterium extorquens	PubMed
685050	White, S.; Boyd, G.; Mathews, F.S.; Xia, Z.X.; Dai, W.W.; Zhang, Y.F.; Davidson, V.L.	The active site structure of the calcium-containing quinoprotein methanol dehydrogenase	Biochemistry	32	12955-12958	1993	Methylophilus sp.	PubMed
685313	Anthony, C.; Williams, P.	The structure and mechanism of methanol dehydrogenase	Biochim. Biophys. Acta	1647	18-23	2003	Methylobacterium extorquens, Methylophilus sp.	PubMed
687417	Kalyuzhnaya, M.G.; Hristova, K.R.; Lidstrom, M.E.; Chistoserdova, L.	Characterization of a novel methanol dehydrogenase in representatives of Burkholderiales: implications for environmental detection of methylotrophy and evidence for convergent evolution	J. Bacteriol.	190	3817-3823	2008	Methylibium petroleiphilum, Methyloversatilis universalis	PubMed
687432	Grosse, S.; Voigt, C.; Wendlandt, K.D.; Kleber, H.P.	Purification and properties of methanol dehydrogenase from Methylosinus sp. WI 14	J. Basic Microbiol.	38	189-196	1998	Methylosinus sp.	PubMed
687486	Xia, Z.X.; Dai, W.W.; Xiong, J.P.; Hao, Z.P.; Davidson, V.L.; White, S.; Mathews, F.S.	The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution	J. Biol. Chem.	267	22289-22297	1992	Methylophilus methylotrophus	PubMed
687993	Jongejan, A.; Jongejan, J.A.; Hagen, W.R.	Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation	J. Comput. Chem.	22	1732-1749	2001	Methylobacterium extorquens, Methylophilus methylotrophus	PubMed
688333	Williams, P.; Coates, L.; Mohammed, F.; Gill, R.; Erskine, P.; Bourgeois, D.; Wood, S.P.; Anthony, C.; Cooper, J.B.	The 1.6A X-ray structure of the unusual c-type cytochrome, cytochrome cL, from the methylotrophic bacterium Methylobacterium extorquens	J. Mol. Biol.	357	151-162	2006	Methylobacterium extorquens	PubMed
689139	Blake, C.C.; Ghosh, M.; Harlos, K.; Avezoux, A.; Anthony, C.	The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues	Nat. Struct. Biol.	1	102-105	1994	Methylobacterium extorquens	PubMed
689815	Zheng, Y.J.; Bruice, T.C.	Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase	Proc. Natl. Acad. Sci. USA	94	11881-11886	1997	Methylophilus methylotrophus	PubMed
689818	Zheng, Y.J.; Xia Zx, Y.J.; Chen Zw, Y.J.; Mathews, F.S.; Bruice, T.C.	Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation	Proc. Natl. Acad. Sci. USA	98	432-434	2001	Methylophilus methylotrophus	PubMed
690095	Ghosh, M.; Anthony, C.; Harlos, K.; Goodwin, M.G.; Blake, C.	The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A	Structure	3	177-187	1995	Methylobacterium extorquens	PubMed
690794	Cozier, G.E.; Giles, I.G.; Anthony, C.	The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens	Biochem. J.	308	375-379	1995	Methylobacterium extorquens	PubMed
712855	Idupulapati, N.B.; Mainardi, D.S.	Quantum chemical modeling of methanol oxidation mechanisms by methanol dehydrogenase enzyme: effect of substitution of calcium by barium in the active site	J. Phys. Chem. A	114	1887-1896	2010	Methylobacterium extorquens	PubMed

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IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

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Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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